Tetramer interface mutations modulate NADK activity. (IMAGE)
Caption
(A) The electronic density of D314 and A330 is presented on the NADK tetramer. (B) NADK WT and indicated mutant plasmids were transfected into HEK293T cells. The cell lysates were cross-linked with BS3. NADK input and cross-linked fractions were detected by immunoblot analyses. (C–E) NADK enzymatic assay with purified NADK WT and indicated mutant proteins from E. coli BL21 strain (n = 3). Michaelis–Menten curve (C), Kcat (D), and Relative catalytic efficiency (E) are presented. (F) ITC binding curves for NADK WT and indicated mutant proteins with substrate molecule NAD+. The Kd values, when measurable, are shown in the figure, while non-measurable values are indicated by NA. Data in (C–E) are presented as mean ± standard deviation; one-way ANOVA; ∗p < 0.05, ∗∗p < 0.01, and ∗∗∗p < 0.001.
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Genes & Diseases
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